Transcriptional Profiling of Black and White Skins Reveals Expression Patterns of mRNA and lncRNA changes for lacking melanocyte in Bama pig
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PROVIDER: PRJNA516660 | ENA |
REPOSITORIES: ENA
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Project description:Skin is the largest organ of body, and one function of skin is protecting underly organs away from ultraviolet (UV) radiation damage. Loss of melanocyte will reduce ability of skin to against UV radiation damage. We found Bama Pig can be an ideal model studying loss of melanocyte. In this study, we performed transcriptome profiling of mRNA and long noncoding RNA in Bama pig white skin (absence of melanocyte) and black skin (existence of melanocyte) to provide dataset for clinical researches. Total of 14,900 mRNAs and 7,566 lncRNAs were expressed in the study. Results of hierarchical cluster analysis and principal component analysis (PCA) demonstrated expression of mRNAs and lncRNAs varied greatly between two color skins. 2,342 mRNA were identified as being differentially expressed, including 1,309 genes that were down-regulated in white skin and 1,033 gene that were up-regulated in white skin (P <0.05; |log2(fold change)| > 1). The genes down-regulated in white skin were associated with melanocyte biology, melanocyte function and keratin, while genes up-regulated in white skin were main associated with metabolism pathway, oxidative phosphorylation and citrate cycle (TCA cycle). In addition, we identified 120 differentially expressed lncRNAs. In those lncRNAs, 4 lncRNAs may function in skin biology (TCONS_00019024 and TCONS_00077733) or metabolic (TCONS_00042201 and TCONS_00060772). Our research provides Bama pig skins datasets and could promote clinical researches utilizing Bama pig as model.
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Project description:In this paper we investigated the mechanism of action of Maganin-2 (Mag-2), a well-known antimicrobial peptide isolated from the African clawed frog Xenopus laevis, by functional proteomic approaches. Several proteins belonging to E. coli macromolecular membrane complexes were identified as Mag-2 putative interactors. Among these, we focused our attention on BamA a membrane protein belonging to the BAM complex responsible for the folding and insertion of nascent β‐barrel Outer Membrane Proteins (OMPs) in the outer membrane. In silico predictions by molecular modelling and in vitro fluorescence binding and Light Scattering experiments carried out using a recombinant form of BamA confirmed the formation of a stable Mag-2/BamA complex and indicated a high affinity of the peptide for BamA. The functional implications of these interactions were investigated by two alternative and complementary approaches. The number of outer membrane proteins OmpA and OmpF produced in E. coli following Mag-2 incubation was evaluated by both western blot analysis and quantitative tandem mass spectrometry in MRM scan mode. In both experiments, a gradual decrease in outer membrane protein production with time was observed because of Mag-2 treatment.
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